Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Mueller‐Cajar, Oliver; Stotz, Mathias; Wendler, Petra; Hartl, F. Ulrich; Bracher, A.; Hayer‐Hartl, Manajit

doi:10.1038/nature10568

Cited by 158 publications

(265 citation statements)

References 60 publications

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“…The nucleotide-bound bacterial RsRca undergoes an oligomeric transition from an ATPase inactive fibril to the functional hexamer, which is triggered by the binding of the allosteric regulator RuBP and provides a regulatory mechanism to respond to increases in Calvin-Benson cycle flux (14). These transitions were earlier demonstrated using negative-stain electron microscopy, but we found they can be recapitulated using gel filtration (Fig.…”

Section: Resultsmentioning

confidence: 55%

“…The bacterial red-type activase RsRca displays ATPase activity only in the presence of the allosteric regulator ribulose 1,5-bisphosphate (RuBP), and the activity is strongly stimulated by its substrate rubisco ( Fig. 1E) (14). No ATPase activity could be detected for CmN and CmP in isolation, whereas both copurified and reconstituted CmNP displayed a low basal ATPase activity that could be stimulated by RuBP and inhibited rubisco.…”

Section: Resultsmentioning

confidence: 99%

“…Three distantly related classes of Rcas (green, red, and CbbQO types) have been identified so far (13)(14)(15)(16). They all belong to the superfamily of AAA + (ATPases associated with various cellular activities) proteins (17) and function as ring-shaped hexamers that couple the energy of ATP hydrolysis to rubisco remodeling.…”

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confidence: 99%

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Characterization of the heterooligomeric red-type rubisco activase from red algae

Loganathan

Tsai

Mueller‐Cajar

2016

Proc. Natl. Acad. Sci. U.S.A.

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The photosynthetic CO 2 -fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) is inhibited by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. Reactivation requires ATP-hydrolysis-powered remodeling of the inhibited complexes by diverse molecular chaperones known as rubisco activases (Rcas). Eukaryotic phytoplankton of the red plastid lineage contain so-called red-type rubiscos, some of which have been shown to possess superior kinetic properties to green-type rubiscos found in higher plants. These organisms are known to encode multiple homologs of CbbX, the α-proteobacterial red-type activase. Here we show that the gene products of two cbbX genes encoded by the nuclear and plastid genomes of the red algae Cyanidioschyzon merolae are nonfunctional in isolation, but together form a thermostable heterooligomeric Rca that can use both α-proteobacterial and red algal-inhibited rubisco complexes as a substrate. The mechanism of rubisco activation appears conserved between the bacterial and the algal systems and involves threading of the rubisco large subunit C terminus. Whereas binding of the allosteric regulator RuBP induces oligomeric transitions to the bacterial activase, it merely enhances the kinetics of ATP hydrolysis in the algal enzyme. Mutational analysis of nuclear and plastid isoforms demonstrates strong coordination between the subunits and implicates the nuclearencoded subunit as being functionally dominant. The plastid-encoded subunit may be catalytically inert. Efforts to enhance crop photosynthesis by transplanting red algal rubiscos with enhanced kinetics will need to take into account the requirement for a compatible Rca.rubisco | activase | photosynthesis | AAA + proteins | red algae

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Section: Resultsmentioning

confidence: 55%

Section: Resultsmentioning

confidence: 99%

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Characterization of the heterooligomeric red-type rubisco activase from red algae

Loganathan

Tsai

Mueller‐Cajar

2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Despite multiple years of research on RubisCO genes and enzymes (Li et al, 1993;Portis, 2003;Mueller-Cajar et al, 2011), still comparatively little knowledge exists about their regulatory mechanisms, assembly or activation. The role that CbbQ (AAA þ ATPase domain) and CbbO (von Willebrand factor, type A) play in prokaryotic RubisCO activation is still enigmatic.…”

Section: Introductionmentioning

confidence: 99%

A function-based screen for seeking RubisCO active clones from metagenomes: novel enzymes influencing RubisCO activity

Böhnke

Perner

2014

The ISME Journal

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) is a key enzyme of the Calvin cycle, which is responsible for most of Earth's primary production. Although research on RubisCO genes and enzymes in plants, cyanobacteria and bacteria has been ongoing for years, still little is understood about its regulation and activation in bacteria. Even more so, hardly any information exists about the function of metagenomic RubisCOs and the role of the enzymes encoded on the flanking DNA owing to the lack of available function-based screens for seeking active RubisCOs from the environment. Here we present the first solely activity-based approach for identifying RubisCO active fosmid clones from a metagenomic library. We constructed a metagenomic library from hydrothermal vent fluids and screened 1056 fosmid clones. Twelve clones exhibited RubisCO activity and the metagenomic fragments resembled genes from Thiomicrospira crunogena. One of these clones was further analyzed. It contained a 35.2 kb metagenomic insert carrying the RubisCO gene cluster and flanking DNA regions. Knockouts of twelve genes and two intergenic regions on this metagenomic fragment demonstrated that the RubisCO activity was significantly impaired and was attributed to deletions in genes encoding putative transcriptional regulators and those believed to be vital for RubisCO activation. Our new technique revealed a novel link between a poorly characterized gene and RubisCO activity. This screen opens the door to directly investigating RubisCO genes and respective enzymes from environmental samples.

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“…Steady progress continues to be made on the structure-function relationships and reaction cycles of chaperones bound to individual client proteins [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16]. In this issue, however, we return to first principles, and shine the spotlight on the role of chaperones in biomolecular assemblies, as first defined for nucleosomes by Laskey [17].…”

Section: Chaperones At the Crossroads Of Life And Deathmentioning

confidence: 99%

Chaperones: needed for both the good times and the bad times

Quinlan

Ellis

2013

Phil. Trans. R. Soc. B

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In this issue, we explore the assembly roles of protein chaperones, mainly through the portal of their associated human diseases (e.g. cardiomyopathy, cataract, neurodegeneration, cancer and neuropathy). There is a diversity to chaperone function that goes beyond the current emphasis in the scientific literature on their undoubted roles in protein folding and refolding. The focus on chaperone-mediated protein folding needs to be broadened by the original Laskey discovery that a chaperone assists the assembly of an oligomeric structure, the nucleosome, and the subsequent suggestion by Ellis that other chaperones may function in assembly processes, as well as in folding. There have been a number of recent discoveries that extend this relatively neglected aspect of chaperone biology to include proteostasis, maintenance of the cellular redox potential, genome stability, transcriptional regulation and cytoskeletal dynamics. So central are these processes that we propose that chaperones stand at the crossroads of life and death because they mediate essential functions, not only during the bad times, but also in the good times. We suggest that chaperones facilitate the success of a species, and hence the evolution of individuals within populations, because of their contributions to so many key cellular processes, of which protein folding is only one.

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Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Cited by 158 publications

References 60 publications

Characterization of the heterooligomeric red-type rubisco activase from red algae

Characterization of the heterooligomeric red-type rubisco activase from red algae

A function-based screen for seeking RubisCO active clones from metagenomes: novel enzymes influencing RubisCO activity

Chaperones: needed for both the good times and the bad times

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